1o5x
From Proteopedia
(New page: 200px<br /><applet load="1o5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o5x, resolution 1.10Å" /> '''Plasmodium falciparu...) |
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| - | [[Image:1o5x.gif|left|200px]]<br /><applet load="1o5x" size=" | + | [[Image:1o5x.gif|left|200px]]<br /><applet load="1o5x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o5x, resolution 1.10Å" /> | caption="1o5x, resolution 1.10Å" /> | ||
'''Plasmodium falciparum TIM complexed to 2-phosphoglycerate'''<br /> | '''Plasmodium falciparum TIM complexed to 2-phosphoglycerate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Triose-phosphate isomerase, a key enzyme of the glycolytic pathway, catalyzes the isomerization of dihydroxy acetone phosphate and | + | Triose-phosphate isomerase, a key enzyme of the glycolytic pathway, catalyzes the isomerization of dihydroxy acetone phosphate and glyceraldehyde 3-phosphate. In this communication we report the crystal structure of Plasmodium falciparum triose-phosphate isomerase complexed to the inhibitor 2-phosphoglycerate at 1.1-A resolution. The crystallographic asymmetric unit contains a dimeric molecule. The inhibitor bound to one of the subunits in which the flexible catalytic loop 6 is in the open conformation has been cleaved into two fragments presumably due to radiation damage. The cleavage products have been tentatively identified as 2-oxoglycerate and meta-phosphate. The intact 2-phosphoglycerate bound to the active site of the other subunit has been observed in two different orientations. The active site loop in this subunit is in both open and "closed" conformations, although the open form is predominant. Concomitant with the loop closure, Phe-96, Leu-167, and residues 208-211 (YGGS) are also observed in dual conformations in the B-subunit. Detailed comparison of the active-site geometry in the present case to the Saccharomyces cerevisiae triose-phosphate isomerase-dihydroxy acetone phosphate and Leishmania mexicana triose-phosphate isomerase-phosphoglycolate complexes, which have also been determined at atomic resolution, shows that certain interactions are common to the three structures, although 2-phosphoglycerate is neither a substrate nor a transition state analogue. |
==About this Structure== | ==About this Structure== | ||
| - | 1O5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with PO3, 3PY and 2PG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http:// | + | 1O5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with <scene name='pdbligand=PO3:'>PO3</scene>, <scene name='pdbligand=3PY:'>3PY</scene> and <scene name='pdbligand=2PG:'>2PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O5X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Balaram, P.]] | [[Category: Balaram, P.]] | ||
[[Category: Eaazhisai, K.]] | [[Category: Eaazhisai, K.]] | ||
| - | [[Category: Murthy, M | + | [[Category: Murthy, M R.]] |
[[Category: Parthasarathy, S.]] | [[Category: Parthasarathy, S.]] | ||
[[Category: 2PG]] | [[Category: 2PG]] | ||
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[[Category: triosephosphate isomerase]] | [[Category: triosephosphate isomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:13:47 2008'' |
Revision as of 12:13, 21 February 2008
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Plasmodium falciparum TIM complexed to 2-phosphoglycerate
Overview
Triose-phosphate isomerase, a key enzyme of the glycolytic pathway, catalyzes the isomerization of dihydroxy acetone phosphate and glyceraldehyde 3-phosphate. In this communication we report the crystal structure of Plasmodium falciparum triose-phosphate isomerase complexed to the inhibitor 2-phosphoglycerate at 1.1-A resolution. The crystallographic asymmetric unit contains a dimeric molecule. The inhibitor bound to one of the subunits in which the flexible catalytic loop 6 is in the open conformation has been cleaved into two fragments presumably due to radiation damage. The cleavage products have been tentatively identified as 2-oxoglycerate and meta-phosphate. The intact 2-phosphoglycerate bound to the active site of the other subunit has been observed in two different orientations. The active site loop in this subunit is in both open and "closed" conformations, although the open form is predominant. Concomitant with the loop closure, Phe-96, Leu-167, and residues 208-211 (YGGS) are also observed in dual conformations in the B-subunit. Detailed comparison of the active-site geometry in the present case to the Saccharomyces cerevisiae triose-phosphate isomerase-dihydroxy acetone phosphate and Leishmania mexicana triose-phosphate isomerase-phosphoglycolate complexes, which have also been determined at atomic resolution, shows that certain interactions are common to the three structures, although 2-phosphoglycerate is neither a substrate nor a transition state analogue.
About this Structure
1O5X is a Single protein structure of sequence from Plasmodium falciparum with , and as ligands. Active as Triose-phosphate isomerase, with EC number 5.3.1.1 Full crystallographic information is available from OCA.
Reference
Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution., Parthasarathy S, Eaazhisai K, Balaram H, Balaram P, Murthy MR, J Biol Chem. 2003 Dec 26;278(52):52461-70. Epub 2003 Oct 16. PMID:14563846
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